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P53739 (FPK1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Flippase kinase 1

EC=2.7.11.1
Gene names
Name:FPK1
Ordered Locus Names:YNR047W
ORF Names:N3449
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length893 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Flippase activator that phosphorylates DFN1 and DFN2 and which is involved in the generation of phospholipid asymmetry in membranes by the inward translocation of phospholipids and in the retrieval pathway from early endosomes to the trans-Golgi network (TGN). Phosphorylates also the N-terminal half of YPK1. Involved in pheromone-response. Ref.3 Ref.7 Ref.10

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Down-regulated by YKP1 phosphorylation. This effect is counteracted in the presence of mannosyl-inositolphosphorylceramide (MIPC). Ref.10

Subcellular location

Cytoplasm. Cell membrane; Peripheral membrane protein Ref.4.

Post-translational modification

The N-terminal non-catalytic domain is phosphorylated by YPK1. Ref.10

Miscellaneous

Present with 752 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. KIN82 subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 893893Flippase kinase 1
PRO_0000086154

Regions

Domain496 – 777282Protein kinase
Domain778 – 86184AGC-kinase C-terminal
Nucleotide binding502 – 5109ATP By similarity

Sites

Active site6211Proton acceptor By similarity
Binding site5251ATP By similarity

Amino acid modifications

Modified residue1401Phosphoserine Ref.8 Ref.9
Modified residue1441Phosphoserine Ref.9
Modified residue1711Phosphoserine Ref.9
Modified residue1751Phosphoserine Ref.9
Modified residue1851Phosphoserine Ref.8
Modified residue3001Phosphoserine Ref.8 Ref.9
Modified residue4141Phosphoserine Ref.6 Ref.8 Ref.9
Modified residue4621Phosphoserine Ref.8 Ref.9

Sequences

Sequence LengthMass (Da)Tools
P53739 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 26AF74EE956F80DB

FASTA893100,546
        10         20         30         40         50         60 
MAGHHHEHEQ ERDHEQEHEH DSLQRPTTGS ERTRSISFSK LLTRSWKRNA SSSNNMSVSS 

        70         80         90        100        110        120 
VNLYSDPENS RESDHNNSGS EGQSSRFSKL KSMFQSGNSS KNASAHNSSQ SSLEGDSASS 

       130        140        150        160        170        180 
SSKLRYVKPM TSVANASPAS PPLSPTIPET DVLQTPKMVH IDQHEHEREH SNCGSPIMLS 

       190        200        210        220        230        240 
SSSFSPTVAR TGTGRRRSPS TPIMPSQNSN NSSSTSAIRP NNYRHHSGSQ GFSSNNPFRE 

       250        260        270        280        290        300 
RAGTVRSSNP YFAYQGLPTH AMSSHDLDEG FQPYANGSGI HFLSTPTSKT NSLTNTKNLS 

       310        320        330        340        350        360 
NLSLNEIKEN EEVQEFNNED FFFHDIPKDL SLKDTLNGSP SRGSSKSPTI TQTFPSIIVG 

       370        380        390        400        410        420 
FDNEYEEDNN NDKHDEKEEQ QTTTDNKTRN LSPTKQNGKA THPRIKIPLR RAASEPNGLQ 

       430        440        450        460        470        480 
LASATSPTSS SARKTSGSSN INDKIPGQSV PPPNSFFPQE PSPKISDFPE PRRSRRLRTK 

       490        500        510        520        530        540 
SFSNKFQDIM VGPQSFEKIR LLGQGDVGKV FLVREKKTNR VYALKVLSKD EMIKRNKIKR 

       550        560        570        580        590        600 
VLTEQEILAT SNHPFIVTLY HSFQSEDYLY LCMEYCMGGE FFRALQTRKT KCICEDDARF 

       610        620        630        640        650        660 
YASEVTAALE YLHLLGFIYR DLKPENILLH QSGHIMLSDF DLSIQAKDSK VPVVKGSAQS 

       670        680        690        700        710        720 
TLVDTKICSD GFRTNSFVGT EEYIAPEVIR GNGHTAAVDW WTLGILIYEM LFGFTPFKGD 

       730        740        750        760        770        780 
NTNETFTNIL KNEVSFPNNN EISRTCKDLI KKLLTKNESK RLGCKMGAAD VKKHPFFKKV 

       790        800        810        820        830        840 
QWSLLRNQEP PLIPVLSEDG YDFAKLSSNK KRQTSQDSHK HLDEQEKNMF EERVEYDDEV 

       850        860        870        880        890 
SEDDPFHDFN SMSLMEQDNN SMIYGNTNSY GKIAYTPNSN RSRSNSHRTF FKR 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. expand/collapse author list , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Identification of novel pheromone-response regulators through systematic overexpression of 120 protein kinases in yeast."
Burchett S.A., Scott A., Errede B., Dohlman H.G.
J. Biol. Chem. 276:26472-26478(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[7]"Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid asymmetry."
Nakano K., Yamamoto T., Kishimoto T., Noji T., Tanaka K.
Mol. Biol. Cell 19:1783-1797(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-185; SER-300; SER-414 AND SER-462, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-144; SER-171; SER-175; SER-300; SER-414 AND SER-462, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"A protein kinase network regulates the function of aminophospholipid flippases."
Roelants F.M., Baltz A.G., Trott A.E., Fereres S., Thorner J.
Proc. Natl. Acad. Sci. U.S.A. 107:34-39(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION BY YPK1, ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z71662 Genomic DNA. Translation: CAA96328.1.
BK006947 Genomic DNA. Translation: DAA10588.1.
PIRS63378.
RefSeqNP_014445.1. NM_001183224.1.

3D structure databases

ProteinModelPortalP53739.
SMRP53739. Positions 420-854.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35872. 80 interactions.
DIPDIP-6427N.
IntActP53739. 6 interactions.
MINTMINT-601192.
STRING4932.YNR047W.

Proteomic databases

MaxQBP53739.
PaxDbP53739.
PRIDEP53739.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNR047W; YNR047W; YNR047W.
GeneID855783.
KEGGsce:YNR047W.

Organism-specific databases

CYGDYNR047w.
SGDS000005330. FPK1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00530000063286.
KOK08286.
OMAGKIAYTP.
OrthoDBEOG7R2BT5.

Enzyme and pathway databases

BioCycYEAST:G3O-33354-MONOMER.

Gene expression databases

GenevestigatorP53739.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR011993. PH_like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio980256.
PROP53739.

Entry information

Entry nameFPK1_YEAST
AccessionPrimary (citable) accession number: P53739
Secondary accession number(s): D6W1M2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 14, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families